PPID Mouse
Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
Greater than 90.0% as determined by SDS-PAGE.
Description
PPID Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-370a.a.) and having a molecular mass of 43.4kDa. PPID is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Cyclophilin-D, a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, plays a crucial role in protein folding. PPIases accelerate the cis-trans isomerization of proline imidic peptide bonds within oligopeptides, thereby facilitating protein folding. Cyclophilin-D exhibits PPIase activity and binds to the immunosuppressive drug cyclosporin-A. Notably, its overexpression is known to suppress apoptosis in cancer cells. This anti-apoptotic effect is mediated through a mitochondrial hexokinase-2 dependent mechanism.
Recombinant Mouse PPID, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 395 amino acids (1-370a.a.). With a molecular weight of 43.4 kDa, this protein is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
The PPID protein solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 1 mM DTT.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To ensure optimal stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. Avoid repeated freeze-thaw cycles.
The purity of the protein is determined to be greater than 90.0% using SDS-PAGE analysis.
The specific activity, defined as the amount of enzyme required to cleave 1 µmol of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin, is greater than 700 nmol/min/mg.
Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
MGSSHHHHHH SSGLVPRGSH MGSEFMSHAS PAAKPSNSKN PRVFFDVDIG GERVGRIVLE LFADIVPKTA ENFRALCTGE KGTGSTTGKP LHFKGCPFHR IIKKFMIQGG DFSNQNGTGG ESIYGEKFED ENFHYKHDRE GLLSMANAGP NTNGSQFFIT TVPTPHLDGK HVVFGQVIKG LGVARTLENV EVNGEKPAKL CVIAECGELK EGDDWGIFPK DGSGDSHPDF PEDADIDLKD VDKILLISED LKNIGNTFFK SQNWEMAIKK YAKVLRYVDS SKAVIEKADR SRLQPIALSC VLNIGACKLK MSNWQGAIDS CLEALEMDPS NTKALYRKAQ GWQGLKEYDQ ALADLKKAQE IAPGDKAIQA ELLKVKQMIK AQKDKEKAVY AKMFA.
Product Science Overview
Peptidylprolyl Isomerase D (PPID), also known as Cyclophilin D, is an enzyme that belongs to the peptidyl-prolyl cis-trans isomerase (PPIase) family. This family of enzymes catalyzes the cis-trans isomerization of proline imidic peptide bonds in polypeptides, which is crucial for protein folding and function .
PPID, like other cyclophilins, forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and is capped by two α-helices at the top and bottom. The β-turns and loops in the strands contribute to the flexibility of the barrel . The primary function of PPID is to facilitate the folding or repair of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds .
PPID is involved in various biological processes, including mitochondrial metabolism, apoptosis, redox regulation, and inflammation. It plays a significant role in diseases and conditions such as ischemic reperfusion injury, AIDS, and cancer . In mice, PPID is expressed in several tissues, including the liver, muscle, and colon .
Recombinant expression of mouse PPID involves cloning the gene into an expression vector, which is then introduced into a host cell, such as E. coli or HEK293T cells. The host cells are cultured, and the recombinant protein is purified using various chromatographic techniques . The recombinant protein is often tagged with a marker, such as MYC/DDK, to facilitate purification and detection .
Recombinant PPID is used in various research applications, including studies on protein folding, signal transduction, and the development of therapeutic agents targeting PPIases. The enzyme’s role in mitochondrial metabolism and apoptosis makes it a valuable tool for studying cellular stress responses and related diseases .
